The NADPH quinone reductase MdaB confers oxidative stress resistance to Helicobacter hepaticus.

Abstract:

:An mdaB mutant strain in a quinone reductase (MdaB) of Helicobacter hepaticus type strain ATCC51449 was constructed by insertional mutagenesis, and the MdaB protein was purified and compared to the Helicobacter pylori enzyme. While wild type H. hepaticus cells could tolerate 6% O(2) for growth, the mdaB strain was clearly inhibited at this oxygen level. Disruption of the gene downstream of mdaB (HH1473) did not affect the oxidative stress phenotype of the strain. The mdaB mutant was also more sensitive to oxidative stress reagents such as H(2)O(2), cumene hydroperoxide, t-butyl hydroperoxide, and paraquat. All H. hepaticus mdaB strains isolated constitutively up-expressed another oxidative stress-combating enzyme, superoxide dismutase; this is in contrast to H. pylori mdaB strains. H. hepaticus MdaB is a flavoprotein catalyzing quinone reduction using a two-electron transfer mechanism from NAD(P)H to quinone. The H. hepaticus enzyme specific activity was far less than for the H. pylori enzyme purified in the same manner.

journal_name

Microb Pathog

journal_title

Microbial pathogenesis

authors

Hong Y,Wang G,Maier RJ

doi

10.1016/j.micpath.2006.08.005

subject

Has Abstract

pub_date

2008-02-01 00:00:00

pages

169-74

issue

2

eissn

0882-4010

issn

1096-1208

pii

S0882-4010(07)00115-5

journal_volume

44

pub_type

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